MolNFT v1 · #94561 · protein
The structure of the camelid antibody CABHUL5 in complex with human lysozyme
4I0C · Lysozyme C: “The structure of the camelid antibody CABHUL5 in complex with human lysozyme”. X-ray diffraction, 1 ligand (CL), 3 pockets (best druggability 0.31). MolNFT v1 #94561 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 4I0C
- Type
- protein
- Length
- 513 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysozyme C; CABHUL5 antibody
- EC
- 3.2.1.17
- UniProt
- P61626
- Ligands
- CL
- Pockets
- 3 · best druggability 0.31
Structure
x-ray diffraction · 3 distinct chains · 19% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Lysozyme C (EC 3.2.1.17) | protein | 130 | 38% helix, 12% strand | P61626 |
| C | CABHUL5 antibody | protein | 126 | 7% helix, 49% strand | — |
| D | CABHUL5 antibody | protein | 127 | 9% helix, 50% strand | — |
Ligands and binding sites
- CL · Chloride ion · ion · 7 copies · chains A, D, B, C
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 70 | 0.31 | 0.74 | 17 | empty |
| 2 | 56 | 0.30 | 0.76 | 14 | GOL |
| 3 | 57 | 0.28 | 0.73 | 13 | empty |
Interfaces
2 interfaces between chains.
- B–C · 705 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 683 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 4I0C · The structure of the camelid antibody cAbHuL5 in complex with human lysozyme · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P61626
- Elsewhere: RCSB PDB 4I0C · PDBe 4I0C · UniProt P61626
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